|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 109, Issue 11 2661-2672, Copyright © 1996 by Company of Biologists
JOURNAL ARTICLES |
M Goedert, CP Baur, J Ahringer, R Jakes, M Hasegawa, MG Spillantini, MJ Smith and F Hill
MRC Laboratory of Molecular Biology, Cambridge, UK.
Tau, MAP2 and MAP4 are structural microtubule-associated proteins (MAPs) that promote the assembly and stability of microtubules. They share three or four imperfect tandem repeats of an amino acid motif, which is involved in the binding to microtubules. All sequences to data containing this motif are of mammalian origin. We report here the cloning and functional characterisation of a new member of this family of proteins from the nematode Caenorhabditis elegans. This protein exists as two isoforms of 413 and 453 amino acids with four or five tandem repeats that are 50% identical to the tau/MAP2/MAP4 repeats. Both isoforms bind to microtubules and promote microtubule assembly, with the five-repeat isoform being more effective at promoting assembly than the four-repeat isoform. When expressed in COS cells, the five-repeat isoform co-localises with microtubules and induces the formation of microtubule bundles, whereas its expression in Sf9 cells leads to the extension of long unipolar processes. In view of its length, amino acid sequence and functional characteristics, we have named this invertebrate structural MAP 'Protein with Tau-Like Repeats' (PTL-1). In C. elegans PTL-1 is expressed in two places known to require microtubule function. It is first seen in the embryonic epidermis, when circumferentially oriented microtubules help to distribute forces generated during elongation. Later, it is found in mechanosensory neurons which contain unusual 15 protofilament microtubules required for the response to touch. These findings indicate that MAPs of the tau/MAP2/MAP4 family are found throughout much of the animal kingdom, where they may play a role in specialised processes requiring microtubules.
This article has been cited by other articles:
![]() |
C. R. Guthrie, G. D. Schellenberg, and B. C. Kraemer SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans Hum. Mol. Genet., May 15, 2009; 18(10): 1825 - 1838. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. C. Kraemer and G. D. Schellenberg SUT-1 enables tau-induced neurotoxicity in C. elegans Hum. Mol. Genet., August 15, 2007; 16(16): 1959 - 1971. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Samsonov, J.-Z. Yu, M. Rasenick, and S. V. Popov Tau interaction with microtubules in vivo J. Cell Sci., December 1, 2004; 117(25): 6129 - 6141. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. AVILA, J. J. LUCAS, M. PEREZ, and F. HERNANDEZ Role of Tau Protein in Both Physiological and Pathological Conditions Physiol Rev, April 1, 2004; 84(2): 361 - 384. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. T. Sinkkonen, M. C. Hanna, E. F. Kirkness, and E. R. Korpi GABAA Receptor epsilon and theta Subunits Display Unusual Structural Variation between Species and Are Enriched in the Rat Locus Ceruleus J. Neurosci., May 15, 2000; 20(10): 3588 - 3595. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Nguyen, D Gruber, and J. Bulinski Microtubule-associated protein 4 (MAP4) regulates assembly, protomer-polymer partitioning and synthesis of tubulin in cultured cells J. Cell Sci., January 6, 1999; 112(12): 1813 - 1824. [Abstract] [PDF] |
||||
![]() |
M. G. Spillantini, J. R. Murrell, M. Goedert, M. R. Farlow, A. Klug, and B. Ghetti Mutation in the tau gene in familial multiple system tauopathy with presenile dementia PNAS, June 23, 1998; 95(13): 7737 - 7741. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Goedert The Neurofibrillary Pathology of Alzheimer's Disease Neuroscientist, March 1, 1997; 3(2): 131 - 141. [Abstract] [PDF] |
||||